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@ARTICLE{Teune:638741,
      author       = {Teune, Michelle and Vieira, Plínio S. and Döhler, Thorben
                      and Palm, Gottfried and Dutschei, Theresa and Bartosik,
                      Daniel and Berndt, Leona and Persinoti, Gabriela F. and
                      Maaß, Sandra and Becher, Dörte and Schweder, Thomas and
                      Murakami, Mario and Lammers, Michael and Bornscheuer, Uwe
                      T.},
      title        = {{I}nsights into a water-mediated catalytic triad
                      architecture in {CE}20 carbohydrate esterases},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2025-04172},
      pages        = {7034},
      year         = {2025},
      abstract     = {Carbohydrate esterases modify polysaccharides by removing
                      different ester moieties thereby affecting their
                      physicochemical properties and their accessibility by
                      glycoside hydrolases. We determined the full-length
                      structures of two members $(Fl8CE20_II$ and $PpCE20_II)$
                      from the carbohydrate esterase family 20 (CE20) by X-ray
                      crystallography that feature an ancillary domain, inserted
                      into the catalytic SGNH-hydrolase domain. Detailed
                      structural analysis identifies a so far undescribed
                      catalytic triad architecture which lacks the typical
                      aspartate for polarization of the histidine but instead
                      reveals a precisely coordinated water molecule mediating
                      contact between the His and Asp. This coordinated water in
                      the Ser-His-(H2O-Asp/Asn) motif, as further confirmed by
                      mutational studies and by determination of kinetic
                      constants, is crucial for catalytic activity. We therefore
                      term this active site architecture a water-mediated
                      catalytic triad.},
      cin          = {EMBL-User},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)277249973 - FOR 2406: Proteogenomik der Marinen
                      Polysaccharid Verwertung (POMPU) (277249973)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)277249973},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40745183},
      doi          = {10.1038/s41467-025-62387-5},
      url          = {https://bib-pubdb1.desy.de/record/638741},
}